ID PFKAM_CANLF Reviewed; 782 AA.
AC P52784;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 13-FEB-2019, entry version 127.
DE RecName: Full=ATP-dependent 6-phosphofructokinase, muscle type {ECO:0000255|HAMAP-Rule:MF_03184};
DE Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_03184};
DE Short=PFK-M;
DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03184};
DE AltName: Full=6-phosphofructokinase type A;
DE AltName: Full=Phosphofructo-1-kinase isozyme A;
DE Short=PFK-A;
DE AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_03184};
GN Name=PFKM; Synonyms=M-PFK;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=8654960; DOI=10.1016/0378-1119(95)00761-X;
RA Smith B.F., Henthorn P.S., Rajpurohit Y., Stedman H., Wolfe J.H.,
RA Patterson D.F., Giger U.;
RT "A cDNA encoding canine muscle-type phosphofructokinase.";
RL Gene 168:275-276(1996).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate
CC to fructose 1,6-bisphosphate by ATP, the first committing step of
CC glycolysis. {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose
CC 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966,
CC ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03184};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or
CC fructose 2,6-bisphosphate, and allosterically inhibited by ATP or
CC citrate. {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- SUBUNIT: Homo- and heterotetramers (By similarity).
CC Phosphofructokinase (PFK) enzyme functions as a tetramer composed
CC of different combinations of 3 types of subunits, called PFKM (M),
CC PFKL (L) and PFKP (P). The composition of the PFK tetramer differs
CC according to the tissue type it is present in. The kinetic and
CC regulatory properties of the tetrameric enzyme are dependent on
CC the subunit composition, hence can vary across tissues (Probable).
CC Interacts (via C-terminus) with HK1 (via N-terminal spermatogenic
CC cell-specific region) (By similarity).
CC {ECO:0000250|UniProtKB:P47857, ECO:0000255|HAMAP-Rule:MF_03184,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- PTM: GlcNAcylation decreases enzyme activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
CC family. ATP-dependent PFK group I subfamily. Eukaryotic two domain
CC clade "E" sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03184}.
DR EMBL; U25183; AAC48615.1; -; mRNA.
DR RefSeq; NP_001003199.1; NM_001003199.1.
DR UniGene; Cfa.3710; -.
DR ProteinModelPortal; P52784; -.
DR SMR; P52784; -.
DR STRING; 9615.ENSCAFP00000013277; -.
DR PaxDb; P52784; -.
DR PRIDE; P52784; -.
DR Ensembl; ENSCAFT00000046392; ENSCAFP00000037674; ENSCAFG00000009035.
DR GeneID; 403849; -.
DR KEGG; cfa:403849; -.
DR CTD; 5213; -.
DR VGNC; VGNC:44447; PFKM.
DR eggNOG; KOG2440; Eukaryota.
DR eggNOG; COG0205; LUCA.
DR GeneTree; ENSGT00940000155440; -.
DR HOGENOM; HOG000200154; -.
DR HOVERGEN; HBG000976; -.
DR InParanoid; P52784; -.
DR KO; K00850; -.
DR OrthoDB; 172878at2759; -.
DR Reactome; R-CFA-70171; Glycolysis.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000002254; Chromosome 27.
DR Bgee; ENSCAFG00000009035; Expressed in 3 organ(s), highest expression level in prefrontal cortex.
DR GO; GO:0005945; C:6-phosphofructokinase complex; IBA:GO_Central.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0097228; C:sperm principal piece; IBA:GO_Central.
DR GO; GO:0003872; F:6-phosphofructokinase activity; ISS:UniProtKB.
DR GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0070095; F:fructose-6-phosphate binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR GO; GO:0061621; P:canonical glycolysis; IBA:GO_Central.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006007; P:glucose catabolic process; IBA:GO_Central.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IBA:GO_Central.
DR HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
DR InterPro; IPR009161; 6-Pfructokinase_euk.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR015912; Phosphofructokinase_CS.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR Pfam; PF00365; PFK; 2.
DR PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 2.
DR TIGRFAMs; TIGR02478; 6PF1K_euk; 1.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Allosteric enzyme; ATP-binding; Complete proteome;
KW Cytoplasm; Glycolysis; Glycoprotein; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P00511}.
FT CHAIN 2 782 ATP-dependent 6-phosphofructokinase,
FT muscle type.
FT /FTId=PRO_0000112014.
FT NP_BIND 88 89 ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
FT NP_BIND 118 121 ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
FT REGION 2 390 N-terminal catalytic PFK domain 1.
FT REGION 164 166 Substrate binding. {ECO:0000255|HAMAP-
FT Rule:MF_03184}.
FT REGION 208 210 Substrate binding. {ECO:0000255|HAMAP-
FT Rule:MF_03184}.
FT REGION 298 301 Substrate binding. {ECO:0000255|HAMAP-
FT Rule:MF_03184}.
FT REGION 391 403 Interdomain linker.
FT REGION 404 782 C-terminal regulatory PFK domain 2.
FT REGION 530 534 Allosteric activator fructose 2,6-
FT bisphosphate binding. {ECO:0000255|HAMAP-
FT Rule:MF_03184}.
FT REGION 575 577 Allosteric activator fructose 2,6-
FT bisphosphate binding. {ECO:0000255|HAMAP-
FT Rule:MF_03184}.
FT REGION 663 666 Allosteric activator fructose 2,6-
FT bisphosphate binding. {ECO:0000255|HAMAP-
FT Rule:MF_03184}.
FT ACT_SITE 166 166 Proton acceptor. {ECO:0000255|HAMAP-
FT Rule:MF_03184}.
FT METAL 119 119 Magnesium; catalytic. {ECO:0000255|HAMAP-
FT Rule:MF_03184}.
FT BINDING 25 25 ATP; via amide nitrogen.
FT {ECO:0000255|HAMAP-Rule:MF_03184}.
FT BINDING 201 201 Substrate; shared with dimeric partner.
FT {ECO:0000255|HAMAP-Rule:MF_03184}.
FT BINDING 264 264 Substrate. {ECO:0000255|HAMAP-
FT Rule:MF_03184}.
FT BINDING 292 292 Substrate; shared with dimeric partner.
FT {ECO:0000255|HAMAP-Rule:MF_03184}.
FT BINDING 473 473 Allosteric activator fructose 2,6-
FT bisphosphate. {ECO:0000255|HAMAP-
FT Rule:MF_03184}.
FT BINDING 568 568 Allosteric activator fructose 2,6-
FT bisphosphate; shared with dimeric
FT partner. {ECO:0000255|HAMAP-
FT Rule:MF_03184}.
FT BINDING 631 631 Allosteric activator fructose 2,6-
FT bisphosphate. {ECO:0000255|HAMAP-
FT Rule:MF_03184}.
FT BINDING 657 657 Allosteric activator fructose 2,6-
FT bisphosphate; shared with dimeric
FT partner. {ECO:0000255|HAMAP-
FT Rule:MF_03184}.
FT BINDING 737 737 Allosteric activator fructose 2,6-
FT bisphosphate. {ECO:0000255|HAMAP-
FT Rule:MF_03184}.
FT MOD_RES 2 2 N-acetylthreonine.
FT {ECO:0000250|UniProtKB:P00511}.
FT MOD_RES 133 133 Phosphoserine.
FT {ECO:0000250|UniProtKB:P47858}.
FT MOD_RES 377 377 Phosphoserine.
FT {ECO:0000250|UniProtKB:P47857}.
FT MOD_RES 669 669 Phosphoserine.
FT {ECO:0000250|UniProtKB:P08237}.
FT MOD_RES 777 777 Phosphoserine.
FT {ECO:0000250|UniProtKB:P00511}.
FT CARBOHYD 532 532 O-linked (GlcNAc) serine. {ECO:0000250}.
SQ SEQUENCE 782 AA; 85561 MW; 7C28514057CFE1C9 CRC64;
MTHEEHHAAK TLGIGKAIAV LTSGGDAQGM NAAVRAVVRV GIFTGARVFF VHEGYQGLVD
GGDHIREATW ESVSMMLQLG GTVIGSARCK DFREREGRLR AAHNLVKRGI TNLCVIGGDG
SLTGADTFRS EWSDLLSDLQ KAGKITAEEA TKSSYLNIVG LVGSIDNDFC GTDMTIGTDS
ALHRIIEIVD AITTTAQSHQ RTFVLEVMGR HCGYLALVTS LSCGADWVFI PECPPDDDWE
EHLCRRLSET RTRGSRLNII IVAEGAIDKN GKPITSEEIK ELVVKRLGYD TRVTVLGHVQ
RGGTPSAFDR ILGSRMGVEA VMALLEGTPD TPACVVSLSG NQAVRLPLME CVQVTKDVTK
AMNDRKFDEA MKLRGRSFMN NWEVYKLLAH IRPPVSKTSA TMHTVAVMNV GAPAAGMNAA
VRSTVRIGLI QGNRVLVVHD GFEGLAKGQI EEAGWSYVGG WTGQGGSKLG TKRTLPKKSF
EQISANITKF NIQGLIIIGG FEAYTGGLEL MEGRKQFDEL CIPFVVIPAT VSNNVPGSDF
SVGADTALNT ICTTCDRIKQ SAAGTKRRVF IIETMGGYCG YLATMAGLAA GADAAYIFEE
PFTIRDLQAN VEHLVQKMKT TVKRGLVLRN EKCNENYTTD FIFNLYSEEG KGIFDSRKNV
LGHMQQGGSP TPFDRNFATK MGAKAMNWMS GKIKESYRNG RIFANTPDSG CVLGMRKRAL
VFQPVTELKD QTDFDHRIPK EQWWLKLRPI LKILAKYEID LDTTEHAHLE HISRKRSGET
SI
//
